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-Structure paper
タイトル | Molecular Organisation of Tick-Borne Encephalitis Virus. |
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ジャーナル・号・ページ | Viruses, Vol. 14, Issue 4, Year 2022 |
掲載日 | 2022年4月11日 |
![]() | Lauri I A Pulkkinen / Sarah V Barrass / Aušra Domanska / Anna K Överby / Maria Anastasina / Sarah J Butcher / ![]() ![]() |
PubMed 要旨 | Tick-borne encephalitis virus (TBEV) is a pathogenic, enveloped, positive-stranded RNA virus in the family . Structural studies of flavivirus virions have primarily focused on mosquito-borne species, ...Tick-borne encephalitis virus (TBEV) is a pathogenic, enveloped, positive-stranded RNA virus in the family . Structural studies of flavivirus virions have primarily focused on mosquito-borne species, with only one cryo-electron microscopy (cryo-EM) structure of a tick-borne species published. Here, we present a 3.3 Å cryo-EM structure of the TBEV virion of the Kuutsalo-14 isolate, confirming the overall organisation of the virus. We observe conformational switching of the peripheral and transmembrane helices of M protein, which can explain the quasi-equivalent packing of the viral proteins and highlights their importance in stabilising membrane protein arrangement in the virion. The residues responsible for M protein interactions are highly conserved in TBEV but not in the structurally studied Hypr strain, nor in mosquito-borne flaviviruses. These interactions may compensate for the lower number of hydrogen bonds between E proteins in TBEV compared to the mosquito-borne flaviviruses. The structure reveals two lipids bound in the E protein which are important for virus assembly. The lipid pockets are comparable to those recently described in mosquito-borne Zika, Spondweni, Dengue, and Usutu viruses. Our results thus advance the understanding of tick-borne flavivirus architecture and virion-stabilising interactions. |
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手法 | EM (単粒子) |
解像度 | 3.3 - 3.5 Å |
構造データ | EMDB-14512, PDB-7z51: ![]() EMDB-14516: Tick-Borne Encephalitis virus Kuutsalo-14 |
化合物 | ![]() ChemComp-CPL: |
由来 |
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![]() | VIRUS / virion / membrane protein / glycoprotein |